Glucomannan Biosynthesis Catalyzed by Pisum sativum Enzymes.
Plant Physiol
; 56(5): 608-12, 1975 Nov.
Article
em En
| MEDLINE
| ID: mdl-16659354
ABSTRACT
The results of molecular weight studies, structural analysis of the [(14)C]polysaccharides, and enzymic properties indicate that the Pisum sativum guanosine diphosphosphate glucose glucosyltransferase is an enzymic component involved in the biosynthesis of glucomannan chains. The properties of the Pisum sativum particulate enzyme are essentially identical to the glucomannan synthetase obtained from Phaseolus aureus. Also present in the particulate preparation is an enzyme which catalyzes the formation of a [(14)C]mannolipid, using guanosine diphosphate-[(14)C]mannose as a substrate. The [(14)C]mannolipid is hydrolyzed by treatment with 0.012 m HCl, but is stable to treatment with 0.09 m NaOH. The formation of the [(14)C]mannolipid is apparently reversed by guanosine diphosphate, but not by guanosine monophosphate. The chromatographic mobility of the [(14)C]mannolipid is identical to that of a similar mannolipid synthesized by a Phaseolus aureus enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
Plant Physiol
Ano de publicação:
1975
Tipo de documento:
Article